HEADER OXIDOREDUCTASE 13-OCT-09 3K7T
TITLE CRYSTAL STRUCTURE OF APO-FORM 6-HYDROXY-L-NICOTINE OXIDASE, CRYSTAL
TITLE 2 FORM P3121
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 6-HYDROXY-L-NICOTINE OXIDASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 1.5.3.5;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ARTHROBACTER NICOTINOVORANS;
SOURCE 3 ORGANISM_TAXID: 29320;
SOURCE 4 GENE: 6-HLNO;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: JM105;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PTRC99A
KEYWDS ENANTIOMERIC SUBSTRATES, FLAVOENZYMES, NICOTINE DEGRADATION, OXIDASE,
KEYWDS 2 OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR G.P.BOURENKOV,G.S.KACHALOVA,H.D.BARTUNIK
REVDAT 4 06-SEP-23 3K7T 1 REMARK
REVDAT 3 01-NOV-17 3K7T 1 REMARK
REVDAT 2 02-MAR-10 3K7T 1 JRNL
REVDAT 1 19-JAN-10 3K7T 0
JRNL AUTH G.S.KACHALOVA,G.P.BOURENKOV,T.MENGESDORF,S.SCHENK,H.R.MAUN,
JRNL AUTH 2 M.BURGHAMMER,C.RIEKEL,K.DECKER,H.D.BARTUNIK
JRNL TITL CRYSTAL STRUCTURE ANALYSIS OF FREE AND SUBSTRATE-BOUND
JRNL TITL 2 6-HYDROXY-L-NICOTINE OXIDASE FROM ARTHROBACTER
JRNL TITL 3 NICOTINOVORANS.
JRNL REF J.MOL.BIOL. V. 396 785 2010
JRNL REFN ISSN 0022-2836
JRNL PMID 20006620
JRNL DOI 10.1016/J.JMB.2009.12.009
REMARK 2
REMARK 2 RESOLUTION. 2.85 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.85
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 16.60
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.1
REMARK 3 NUMBER OF REFLECTIONS : 38462
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.278
REMARK 3 R VALUE (WORKING SET) : 0.275
REMARK 3 FREE R VALUE : 0.321
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2035
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.85
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.92
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2792
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.22
REMARK 3 BIN R VALUE (WORKING SET) : 0.4360
REMARK 3 BIN FREE R VALUE SET COUNT : 134
REMARK 3 BIN FREE R VALUE : 0.4570
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6540
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 192
REMARK 3 SOLVENT ATOMS : 42
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 72.90
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 72.94
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 3.72000
REMARK 3 B22 (A**2) : 3.72000
REMARK 3 B33 (A**2) : -5.58000
REMARK 3 B12 (A**2) : 1.86000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.621
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.393
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.345
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 18.930
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.927
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.895
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6890 ; 0.018 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 9374 ; 1.781 ; 1.990
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 848 ; 7.599 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 306 ;36.675 ;23.595
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1054 ;18.815 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 50 ;17.515 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1030 ; 0.103 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5236 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 3139 ; 0.233 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 4594 ; 0.322 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 237 ; 0.167 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 34 ; 0.294 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 3 ; 0.161 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 4286 ; 1.021 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 6750 ; 1.853 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2979 ; 2.467 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2624 ; 4.256 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3K7T COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-OCT-09.
REMARK 100 THE DEPOSITION ID IS D_1000055654.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-DEC-02
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : MPG/DESY, HAMBURG
REMARK 200 BEAMLINE : BW6
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.05
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MAR CCD 165 MM
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 41084
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.850
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 200 DATA REDUNDANCY : 7.500
REMARK 200 R MERGE (I) : 0.07800
REMARK 200 R SYM (I) : 0.07800
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 25.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.85
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.90
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 7.50
REMARK 200 R MERGE FOR SHELL (I) : 0.75000
REMARK 200 R SYM FOR SHELL (I) : 0.75000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLREP
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 3K7M
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 73.84
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.70
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M HEPES, 1.5M LITHIUM SULFATE, PH
REMARK 280 7.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 289K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+2/3
REMARK 290 6555 -X,-X+Y,-Z+1/3
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 66.63933
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 133.27867
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 133.27867
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 66.63933
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1130 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 33560 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 SER A 425 CB OG
REMARK 470 SER B 425 CB OG
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 PRO B 370 C - N - CD ANGL. DEV. = -12.7 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 LEU A 92 45.05 -97.53
REMARK 500 LYS A 129 -147.53 -84.99
REMARK 500 HIS A 187 56.49 -94.31
REMARK 500 TYR A 189 70.10 40.72
REMARK 500 SER A 232 -81.34 -54.91
REMARK 500 LYS A 241 -82.67 -12.95
REMARK 500 ASP A 242 71.35 -67.09
REMARK 500 HIS A 244 179.24 -53.40
REMARK 500 ALA A 254 41.62 -108.79
REMARK 500 TYR A 313 -71.36 -105.89
REMARK 500 SER A 317 -157.50 -151.45
REMARK 500 PHE A 367 -50.53 -133.75
REMARK 500 PRO A 370 -76.04 -95.13
REMARK 500 HIS A 383 -55.24 -155.43
REMARK 500 ASP B 135 63.95 60.60
REMARK 500 ASP B 151 85.21 57.11
REMARK 500 HIS B 187 42.01 -87.83
REMARK 500 LEU B 196 42.82 -80.72
REMARK 500 LEU B 198 81.30 -68.52
REMARK 500 ASP B 199 -81.86 -106.58
REMARK 500 TYR B 313 -70.77 -100.47
REMARK 500 THR B 327 -157.63 -158.87
REMARK 500 PHE B 367 -51.13 -130.77
REMARK 500 PRO B 370 -88.76 -108.32
REMARK 500 HIS B 383 -72.06 -140.39
REMARK 500 ALA B 390 54.36 -102.98
REMARK 500 PHE B 404 79.41 -151.40
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 GP7 A 435
REMARK 610 GP7 B 435
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD A 434
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GP7 A 435
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD B 434
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GP7 B 435
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3K7M RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF 6-HYDROXY-L-NICOTINE OXIDASE FROM ARTHROBACTER
REMARK 900 NICOTINOVORANS
REMARK 900 RELATED ID: 3K7Q RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF SUBSTRATE-BOUND 6-HYDROXY-L-NICOTINE OXIDASE
REMARK 900 FROM ARTHROBACTER NICOTINOVORANS
DBREF 3K7T A 1 425 UNP Q93NH4 Q93NH4_ARTNI 1 425
DBREF 3K7T B 1 425 UNP Q93NH4 Q93NH4_ARTNI 1 425
SEQRES 1 A 425 MET TYR ASP ALA ILE VAL VAL GLY GLY GLY PHE SER GLY
SEQRES 2 A 425 LEU LYS ALA ALA ARG ASP LEU THR ASN ALA GLY LYS LYS
SEQRES 3 A 425 VAL LEU LEU LEU GLU GLY GLY GLU ARG LEU GLY GLY ARG
SEQRES 4 A 425 ALA TYR SER ARG GLU SER ARG ASN VAL PRO GLY LEU ARG
SEQRES 5 A 425 VAL GLU ILE GLY GLY ALA TYR LEU HIS ARG LYS HIS HIS
SEQRES 6 A 425 PRO ARG LEU ALA ALA GLU LEU ASP ARG TYR GLY ILE PRO
SEQRES 7 A 425 THR ALA ALA ALA SER GLU PHE THR SER PHE ARG HIS ARG
SEQRES 8 A 425 LEU GLY PRO THR ALA VAL ASP GLN ALA PHE PRO ILE PRO
SEQRES 9 A 425 GLY SER GLU ALA VAL ALA VAL GLU ALA ALA THR TYR THR
SEQRES 10 A 425 LEU LEU ARG ASP ALA HIS ARG ILE ASP LEU GLU LYS GLY
SEQRES 11 A 425 LEU GLU ASN GLN ASP LEU GLU ASP LEU ASP ILE PRO LEU
SEQRES 12 A 425 ASN GLU TYR VAL ASP LYS LEU ASP LEU PRO PRO VAL SER
SEQRES 13 A 425 ARG GLN PHE LEU LEU ALA TRP ALA TRP ASN MET LEU GLY
SEQRES 14 A 425 GLN PRO ALA ASP GLN ALA SER ALA LEU TRP MET LEU GLN
SEQRES 15 A 425 LEU VAL ALA ALA HIS HIS TYR SER ILE LEU GLY VAL VAL
SEQRES 16 A 425 LEU SER LEU ASP GLU VAL PHE SER ASN GLY SER ALA ASP
SEQRES 17 A 425 LEU VAL ASP ALA MET SER GLN GLU ILE PRO GLU ILE ARG
SEQRES 18 A 425 LEU GLN THR VAL VAL THR GLY ILE ASP GLN SER GLY ASP
SEQRES 19 A 425 VAL VAL ASN VAL THR VAL LYS ASP GLY HIS ALA PHE GLN
SEQRES 20 A 425 ALA HIS SER VAL ILE VAL ALA THR PRO MET ASN THR TRP
SEQRES 21 A 425 ARG ARG ILE VAL PHE THR PRO ALA LEU PRO GLU ARG ARG
SEQRES 22 A 425 ARG SER VAL ILE GLU GLU GLY HIS GLY GLY GLN GLY LEU
SEQRES 23 A 425 LYS ILE LEU ILE HIS VAL ARG GLY ALA GLU ALA GLY ILE
SEQRES 24 A 425 GLU CYS VAL GLY ASP GLY ILE PHE PRO THR LEU TYR ASP
SEQRES 25 A 425 TYR CYS GLU VAL SER GLU SER GLU ARG LEU LEU VAL ALA
SEQRES 26 A 425 PHE THR ASP SER GLY SER PHE ASP PRO THR ASP ILE GLY
SEQRES 27 A 425 ALA VAL LYS ASP ALA VAL LEU TYR TYR LEU PRO GLU VAL
SEQRES 28 A 425 GLU VAL LEU GLY ILE ASP TYR HIS ASP TRP ILE ALA ASP
SEQRES 29 A 425 PRO LEU PHE GLU GLY PRO TRP VAL ALA PRO ARG VAL GLY
SEQRES 30 A 425 GLN PHE SER ARG VAL HIS LYS GLU LEU GLY GLU PRO ALA
SEQRES 31 A 425 GLY ARG ILE HIS PHE VAL GLY SER ASP VAL SER LEU GLU
SEQRES 32 A 425 PHE PRO GLY TYR ILE GLU GLY ALA LEU GLU THR ALA GLU
SEQRES 33 A 425 CYS ALA VAL ASN ALA ILE LEU HIS SER
SEQRES 1 B 425 MET TYR ASP ALA ILE VAL VAL GLY GLY GLY PHE SER GLY
SEQRES 2 B 425 LEU LYS ALA ALA ARG ASP LEU THR ASN ALA GLY LYS LYS
SEQRES 3 B 425 VAL LEU LEU LEU GLU GLY GLY GLU ARG LEU GLY GLY ARG
SEQRES 4 B 425 ALA TYR SER ARG GLU SER ARG ASN VAL PRO GLY LEU ARG
SEQRES 5 B 425 VAL GLU ILE GLY GLY ALA TYR LEU HIS ARG LYS HIS HIS
SEQRES 6 B 425 PRO ARG LEU ALA ALA GLU LEU ASP ARG TYR GLY ILE PRO
SEQRES 7 B 425 THR ALA ALA ALA SER GLU PHE THR SER PHE ARG HIS ARG
SEQRES 8 B 425 LEU GLY PRO THR ALA VAL ASP GLN ALA PHE PRO ILE PRO
SEQRES 9 B 425 GLY SER GLU ALA VAL ALA VAL GLU ALA ALA THR TYR THR
SEQRES 10 B 425 LEU LEU ARG ASP ALA HIS ARG ILE ASP LEU GLU LYS GLY
SEQRES 11 B 425 LEU GLU ASN GLN ASP LEU GLU ASP LEU ASP ILE PRO LEU
SEQRES 12 B 425 ASN GLU TYR VAL ASP LYS LEU ASP LEU PRO PRO VAL SER
SEQRES 13 B 425 ARG GLN PHE LEU LEU ALA TRP ALA TRP ASN MET LEU GLY
SEQRES 14 B 425 GLN PRO ALA ASP GLN ALA SER ALA LEU TRP MET LEU GLN
SEQRES 15 B 425 LEU VAL ALA ALA HIS HIS TYR SER ILE LEU GLY VAL VAL
SEQRES 16 B 425 LEU SER LEU ASP GLU VAL PHE SER ASN GLY SER ALA ASP
SEQRES 17 B 425 LEU VAL ASP ALA MET SER GLN GLU ILE PRO GLU ILE ARG
SEQRES 18 B 425 LEU GLN THR VAL VAL THR GLY ILE ASP GLN SER GLY ASP
SEQRES 19 B 425 VAL VAL ASN VAL THR VAL LYS ASP GLY HIS ALA PHE GLN
SEQRES 20 B 425 ALA HIS SER VAL ILE VAL ALA THR PRO MET ASN THR TRP
SEQRES 21 B 425 ARG ARG ILE VAL PHE THR PRO ALA LEU PRO GLU ARG ARG
SEQRES 22 B 425 ARG SER VAL ILE GLU GLU GLY HIS GLY GLY GLN GLY LEU
SEQRES 23 B 425 LYS ILE LEU ILE HIS VAL ARG GLY ALA GLU ALA GLY ILE
SEQRES 24 B 425 GLU CYS VAL GLY ASP GLY ILE PHE PRO THR LEU TYR ASP
SEQRES 25 B 425 TYR CYS GLU VAL SER GLU SER GLU ARG LEU LEU VAL ALA
SEQRES 26 B 425 PHE THR ASP SER GLY SER PHE ASP PRO THR ASP ILE GLY
SEQRES 27 B 425 ALA VAL LYS ASP ALA VAL LEU TYR TYR LEU PRO GLU VAL
SEQRES 28 B 425 GLU VAL LEU GLY ILE ASP TYR HIS ASP TRP ILE ALA ASP
SEQRES 29 B 425 PRO LEU PHE GLU GLY PRO TRP VAL ALA PRO ARG VAL GLY
SEQRES 30 B 425 GLN PHE SER ARG VAL HIS LYS GLU LEU GLY GLU PRO ALA
SEQRES 31 B 425 GLY ARG ILE HIS PHE VAL GLY SER ASP VAL SER LEU GLU
SEQRES 32 B 425 PHE PRO GLY TYR ILE GLU GLY ALA LEU GLU THR ALA GLU
SEQRES 33 B 425 CYS ALA VAL ASN ALA ILE LEU HIS SER
HET FAD A 434 53
HET GP7 A 435 43
HET FAD B 434 53
HET GP7 B 435 43
HETNAM FAD FLAVIN-ADENINE DINUCLEOTIDE
HETNAM GP7 (1R)-2-{[(S)-(2-AMINOETHOXY)(HYDROXY)PHOSPHORYL]OXY}-1-
HETNAM 2 GP7 [(PENTADECANOYLOXY)METHYL]ETHYL (12E)-HEXADECA-9,12-
HETNAM 3 GP7 DIENOATE
HETSYN GP7 1-PENTADECANOYL-2-HEXADECANOYL-SN-GLYCERO-3-
HETSYN 2 GP7 PHOSPHOETHANOLAMINE
FORMUL 3 FAD 2(C27 H33 N9 O15 P2)
FORMUL 4 GP7 2(C36 H68 N O8 P)
FORMUL 7 HOH *42(H2 O)
HELIX 1 1 GLY A 10 GLY A 24 1 15
HELIX 2 2 HIS A 65 GLY A 76 1 12
HELIX 3 3 GLU A 107 ARG A 124 1 18
HELIX 4 4 LEU A 136 ASP A 140 5 5
HELIX 5 5 PRO A 142 ASP A 151 1 10
HELIX 6 6 PRO A 153 LEU A 168 1 16
HELIX 7 7 SER A 176 HIS A 187 1 12
HELIX 8 8 SER A 206 GLN A 215 1 10
HELIX 9 9 PRO A 256 ILE A 263 5 8
HELIX 10 10 PRO A 270 GLY A 280 1 11
HELIX 11 11 ASP A 336 TYR A 346 1 11
HELIX 12 12 GLY A 377 VAL A 382 1 6
HELIX 13 13 LYS A 384 GLU A 388 5 5
HELIX 14 14 TYR A 407 HIS A 424 1 18
HELIX 15 15 GLY B 10 GLY B 24 1 15
HELIX 16 16 HIS B 65 ASP B 73 1 9
HELIX 17 17 PRO B 104 SER B 106 5 3
HELIX 18 18 GLU B 107 ARG B 124 1 18
HELIX 19 19 PRO B 142 ASP B 151 1 10
HELIX 20 20 PRO B 153 GLY B 169 1 17
HELIX 21 21 SER B 176 HIS B 187 1 12
HELIX 22 22 ILE B 191 LEU B 196 1 6
HELIX 23 23 SER B 206 GLN B 215 1 10
HELIX 24 24 PRO B 256 TRP B 260 5 5
HELIX 25 25 PRO B 270 GLU B 278 1 9
HELIX 26 26 ASP B 336 TYR B 346 1 11
HELIX 27 27 GLY B 377 VAL B 382 1 6
HELIX 28 28 HIS B 383 GLU B 388 5 6
HELIX 29 29 TYR B 407 HIS B 424 1 18
SHEET 1 A 7 ILE A 220 ARG A 221 0
SHEET 2 A 7 VAL A 27 LEU A 30 1 N LEU A 29 O ARG A 221
SHEET 3 A 7 TYR A 2 VAL A 7 1 N VAL A 6 O LEU A 28
SHEET 4 A 7 ALA A 245 VAL A 253 1 O ILE A 252 N VAL A 7
SHEET 5 A 7 VAL A 236 VAL A 240 -1 N VAL A 238 O PHE A 246
SHEET 6 A 7 VAL A 226 ASP A 230 -1 N ASP A 230 O ASN A 237
SHEET 7 A 7 VAL A 264 THR A 266 1 O VAL A 264 N THR A 227
SHEET 1 B 5 ILE A 220 ARG A 221 0
SHEET 2 B 5 VAL A 27 LEU A 30 1 N LEU A 29 O ARG A 221
SHEET 3 B 5 TYR A 2 VAL A 7 1 N VAL A 6 O LEU A 28
SHEET 4 B 5 ALA A 245 VAL A 253 1 O ILE A 252 N VAL A 7
SHEET 5 B 5 ILE A 393 PHE A 395 1 O HIS A 394 N VAL A 251
SHEET 1 C 2 SER A 42 GLU A 44 0
SHEET 2 C 2 ARG A 52 GLU A 54 -1 O VAL A 53 N ARG A 43
SHEET 1 D 2 THR A 79 ALA A 81 0
SHEET 2 D 2 GLU A 200 PHE A 202 -1 O VAL A 201 N ALA A 80
SHEET 1 E 6 SER A 87 PHE A 88 0
SHEET 2 E 6 ILE A 299 VAL A 302 1 O GLU A 300 N SER A 87
SHEET 3 E 6 THR A 309 GLU A 315 -1 O LEU A 310 N CYS A 301
SHEET 4 E 6 GLU A 320 ASP A 328 -1 O LEU A 322 N TYR A 313
SHEET 5 E 6 GLY A 285 ARG A 293 -1 N LEU A 286 O THR A 327
SHEET 6 E 6 GLU A 352 TYR A 358 -1 O LEU A 354 N HIS A 291
SHEET 1 F 7 GLU B 219 ARG B 221 0
SHEET 2 F 7 VAL B 27 LEU B 30 1 N LEU B 29 O GLU B 219
SHEET 3 F 7 TYR B 2 VAL B 7 1 N VAL B 6 O LEU B 28
SHEET 4 F 7 PHE B 246 VAL B 253 1 O ILE B 252 N VAL B 7
SHEET 5 F 7 VAL B 236 VAL B 240 -1 N VAL B 238 O PHE B 246
SHEET 6 F 7 VAL B 226 ASP B 230 -1 N ASP B 230 O ASN B 237
SHEET 7 F 7 VAL B 264 THR B 266 1 O VAL B 264 N ILE B 229
SHEET 1 G 5 GLU B 219 ARG B 221 0
SHEET 2 G 5 VAL B 27 LEU B 30 1 N LEU B 29 O GLU B 219
SHEET 3 G 5 TYR B 2 VAL B 7 1 N VAL B 6 O LEU B 28
SHEET 4 G 5 PHE B 246 VAL B 253 1 O ILE B 252 N VAL B 7
SHEET 5 G 5 ILE B 393 PHE B 395 1 O HIS B 394 N VAL B 251
SHEET 1 H 2 SER B 42 GLU B 44 0
SHEET 2 H 2 ARG B 52 GLU B 54 -1 O VAL B 53 N ARG B 43
SHEET 1 I 2 THR B 79 ALA B 81 0
SHEET 2 I 2 GLU B 200 PHE B 202 -1 O VAL B 201 N ALA B 80
SHEET 1 J 6 SER B 87 PHE B 88 0
SHEET 2 J 6 ILE B 299 VAL B 302 1 O GLU B 300 N SER B 87
SHEET 3 J 6 THR B 309 GLU B 315 -1 O ASP B 312 N ILE B 299
SHEET 4 J 6 GLU B 320 ASP B 328 -1 O VAL B 324 N TYR B 311
SHEET 5 J 6 GLY B 285 ARG B 293 -1 N VAL B 292 O ARG B 321
SHEET 6 J 6 GLU B 352 TYR B 358 -1 O LEU B 354 N HIS B 291
CISPEP 1 THR A 266 PRO A 267 0 -3.01
CISPEP 2 HIS B 244 ALA B 245 0 2.20
CISPEP 3 THR B 266 PRO B 267 0 -2.06
SITE 1 AC1 28 GLY A 8 GLY A 10 PHE A 11 SER A 12
SITE 2 AC1 28 LEU A 30 GLU A 31 GLY A 32 GLY A 37
SITE 3 AC1 28 GLY A 38 ARG A 39 ALA A 40 GLY A 56
SITE 4 AC1 28 GLY A 57 TYR A 59 THR A 224 VAL A 226
SITE 5 AC1 28 ALA A 254 THR A 255 PRO A 256 LEU A 366
SITE 6 AC1 28 PHE A 367 TRP A 371 GLY A 397 SER A 398
SITE 7 AC1 28 GLY A 406 TYR A 407 ILE A 408 ALA A 411
SITE 1 AC2 12 GLN A 99 ALA A 100 THR A 115 PHE A 159
SITE 2 AC2 12 LEU A 160 MET A 180 ILE A 191 LEU A 192
SITE 3 AC2 12 VAL A 195 ILE B 103 GLY B 105 ALA B 108
SITE 1 AC3 32 VAL B 7 GLY B 8 GLY B 10 PHE B 11
SITE 2 AC3 32 SER B 12 LEU B 30 GLU B 31 GLY B 32
SITE 3 AC3 32 GLY B 37 GLY B 38 ARG B 39 GLY B 56
SITE 4 AC3 32 GLY B 57 TYR B 59 THR B 224 VAL B 225
SITE 5 AC3 32 VAL B 226 ALA B 254 THR B 255 PRO B 256
SITE 6 AC3 32 ILE B 263 TRP B 361 LEU B 366 PHE B 367
SITE 7 AC3 32 PRO B 370 GLY B 397 SER B 398 GLY B 406
SITE 8 AC3 32 TYR B 407 ILE B 408 ALA B 411 HOH B 519
SITE 1 AC4 12 ILE A 103 PRO A 104 GLY A 105 ALA B 100
SITE 2 AC4 12 VAL B 111 THR B 115 PHE B 159 LEU B 160
SITE 3 AC4 12 MET B 180 ILE B 191 LEU B 192 VAL B 195
CRYST1 122.957 122.957 199.918 90.00 90.00 120.00 P 31 2 1 12
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.008133 0.004696 0.000000 0.00000
SCALE2 0.000000 0.009391 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005002 0.00000
(ATOM LINES ARE NOT SHOWN.)
END